[Lys(Ac)27]-Histone H3 (23-34)

Product Name: [Lys(Ac)27]-Histone H3 (23-34)

Sequence One Letter Code: KAAR-K(Ac)-SAPATGG

Sequence Three Letter Code: H-Lys-Ala-Ala-Arg-Lys(Ac)-Ser-Ala-Pro-Ala-Thr-Gly-Gly-OH

Chemical Formula:C48H85N17O16

Molecular Weight: 1156.4

Purity: 95%

Form: Lyophilized

Storage Conditions: - 20 °C

Research Area: epigenetics

Source / Species: human

Conjugation: Unconjugated

Code Nacres: NA.26

Application: Histone H3 (23–34) K27Ac is a synthetic peptide corresponding to residues 23–34 of histone H3 with acetylation at lysine 27. Acetylation at H3K27 is an epigenetic modification associated with chromatin dynamics and transcriptional regulation. Although present at relatively low abundance compared with other acetylation marks, H3K27 acetylation has been linked to histone deposition events during DNA replication and chromatin assembly. This peptide preserves the native sequence context surrounding the modification site, allowing researchers to investigate recognition by acetyl-lysine binding domains such as bromodomains. It is commonly used in biochemical and biophysical assays to study acetylation-dependent protein interactions, chromatin remodeling mechanisms, and the role of H3K27 acetylation in regulating transcription and replication-associated chromatin states.

Current Research: Histone acetylation is one of the most extensively studied epigenetic modifications involved in regulating chromatin structure and gene expression. By neutralizing the positive charge of lysine residues on histone tails, acetylation can weaken histone–DNA interactions and create binding sites for specialized chromatin-associated proteins. Among these modifications, acetylation at lysine 27 of histone H3 (H3K27Ac) has gained significant attention due to its role in chromatin dynamics and transcriptional regulation. The Histone H3 (23–34) K27Ac peptide is a synthetic peptide representing residues 23–34 of histone H3 with site-specific acetylation at lysine 27. By preserving the natural sequence surrounding the modification site, this peptide serves as a valuable model substrate for investigating acetylation-dependent chromatin interactions and regulatory mechanisms. Histone H3 and Chromatin Organization Histone H3 is a central component of nucleosomes, the structural units that package DNA into chromatin. Within each nucleosome, approximately 147 base pairs of DNA wrap around an octamer composed of two copies each of histones H2A, H2B, H3, and H4. The histone proteins contain flexible N-terminal tails and structured domains that can undergo numerous post-translational modifications (PTMs). These modifications—including acetylation, methylation, phosphorylation, and ubiquitination—form part of the epigenetic regulatory system often referred to as the histone code. Specific combinations of histone marks influence how chromatin-binding proteins interact with nucleosomes, ultimately affecting transcription, replication, and DNA repair processes. The region surrounding lysine 27 on histone H3 is an important regulatory hotspot. Modifications at this site can alter chromatin accessibility and help coordinate gene expression programs during development and cellular differentiation. Biological Significance of H3K27 Acetylation Acetylation of histone H3 at lysine 27 (H3K27Ac) is widely associated with transcriptionally active chromatin. This modification is often found at active enhancers and promoters, where it contributes to the recruitment of transcriptional machinery and chromatin remodeling complexes. The addition of an acetyl group neutralizes the positive charge on lysine, reducing electrostatic interactions between histones and DNA. This effect promotes a more relaxed chromatin structure that facilitates access to regulatory proteins involved in gene expression. Although H3K27 acetylation is typically less abundant than some other histone acetylation marks, it plays a distinct role in chromatin regulation. Studies have linked this modification to histone deposition events during DNA replication and chromatin assembly, suggesting that H3K27Ac contributes to the establishment of newly formed chromatin states following DNA synthesis. The presence of H3K27Ac can also influence the recruitment of specific chromatin-associated proteins that recognize acetylated lysine residues, thereby coordinating downstream regulatory pathways. Recognition by Acetyl-Lysine Binding Domains Acetylated histone residues serve as docking sites for specialized protein domains that recognize acetyl-lysine modifications. One of the most important families of such domains is the bromodomain family. Bromodomains are present in many chromatin-associated proteins, including transcriptional coactivators, chromatin remodelers, and histone acetyltransferase complexes. These domains specifically bind acetylated lysine residues within histone tails and help recruit regulatory proteins to active chromatin regions. By reproducing the native sequence context surrounding H3K27, the Histone H3 (23–34) K27Ac peptide provides a reliable platform for studying how bromodomains and other acetyl-lysine recognition domains interact with acetylated histone substrates. Advantages of Using Synthetic Histone Peptides Synthetic histone peptides offer several advantages for epigenetics research. Unlike full nucleosomes or chromatin extracts, peptides provide a well-defined and simplified system for analyzing individual histone modifications. The Histone H3 (23–34) K27Ac peptide preserves the local amino acid sequence surrounding the acetylated lysine residue while eliminating structural complexity. This allows researchers to examine modification-specific protein interactions with greater precision. Such peptides are commonly used in: Binding assays to study acetylation-dependent protein interactions Bromodomain screening experiments Chromatin remodeling studies Biophysical analyses of histone recognition mechanisms These experimental approaches help reveal how specific histone modifications regulate chromatin structure and transcriptional activity. Applications in Epigenetics and Chromatin Research The Histone H3 (23–34) K27Ac peptide is widely used in studies focused on understanding how acetylation contributes to chromatin regulation. Its defined modification state makes it suitable for investigating multiple aspects of epigenetic signaling. Typical applications include: Protein–peptide interaction studies Researchers use the peptide to identify proteins that recognize acetylated histone H3 sequences. Bromodomain binding assays The peptide provides a substrate for examining how bromodomain-containing proteins interact with H3K27Ac. Chromatin remodeling research Understanding how acetylated histone tails influence chromatin accessibility can reveal mechanisms that control transcription. Replication-associated chromatin studies The peptide can help explore the role of H3K27 acetylation in histone deposition and chromatin assembly following DNA replication. Supporting Research on Epigenetic Regulation The regulation of chromatin structure involves a coordinated network of histone modifications and protein interactions. Acetylation marks such as H3K27Ac play an important role in defining active chromatin states and guiding the recruitment of transcriptional regulators. The Histone H3 (23–34) K27Ac peptide provides a practical experimental model for studying these processes. By preserving the natural sequence context around the acetylated lysine residue, the peptide enables researchers to examine acetylation-dependent protein recognition and chromatin remodeling mechanisms in a controlled setting. Through applications in biochemical assays and chromatin interaction studies, this peptide supports ongoing efforts to understand how histone acetylation contributes to transcriptional regulation and chromatin dynamics.